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Q0UZK0 (KYNU2_PHANO) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Kynureninase 2
EC=3.7.1.3
Alternative name(s):
Biosynthesis of nicotinic acid protein 5-2
L-kynurenine hydrolase 2
Gene names
Name:BNA5-2
ORF Names:SNOG_02814
OrganismPhaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume blotch fungus) (Septoria nodorum) [Reference proteome]
Taxonomic identifier321614 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Dothideomycetes › Pleosporomycetidae › Pleosporales › Pleosporineae › Phaeosphaeriaceae › Phaeosphaeria ›

Protein attributes

Sequence length489 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively By similarity. HAMAP-Rule MF_03017

Catalytic activity

L-kynurenine + H2O = anthranilate + L-alanine. HAMAP-Rule MF_03017

L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine. HAMAP-Rule MF_03017

Cofactor

Pyridoxal phosphate By similarity.

Pathway

Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1. HAMAP-Rule MF_03017

Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3. HAMAP-Rule MF_03017

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the kynureninase family.

Ontologies

Keywords
   Biological processPyridine nucleotide biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-kynurenine catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

NAD biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

tryptophan catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionkynureninase activity

Inferred from electronic annotation. Source: EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 489489Kynureninase 2 HAMAP-Rule MF_03017
PRO_0000356983

Regions

Region177 – 1804Pyridoxal phosphate binding By similarity

Sites

Binding site1491Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1501Pyridoxal phosphate By similarity
Binding site2611Pyridoxal phosphate By similarity
Binding site2641Pyridoxal phosphate By similarity
Binding site2861Pyridoxal phosphate By similarity
Binding site3171Pyridoxal phosphate By similarity
Binding site3451Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2871N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0UZK0 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 4F2FBB290F1825BE

FASTA48954,097
        10         20         30         40         50         60 
MDASAAISQL RQGQKPEWPQ NANTSDFAKT LDNSSEFPKT LRHEYVVPTK AQLKRKTLND 

        70         80         90        100        110        120 
DAQTAAKASS SDDEGIYFCG NSLGLQPKAV GEYLNAYLKT WGSIAVGSHF TPMADSPLTP 

       130        140        150        160        170        180 
FQDMAAECAR RMSDIVGASP SEIVAMNTLT INLHLMMAAF YKPTEKKHKI MCEWRPFPSD 

       190        200        210        220        230        240 
WYAIESQIEW HGLDPKKSML LVKPDDGYLM TTESILKLID QEADELALIM LPGIQYYSGQ 

       250        260        270        280        290        300 
LLDIPTITTH ARKHGITIGW DLAHAAGNVE LKLHDWDVDF ACWCTYKYMN AGAGAIAGAF 

       310        320        330        340        350        360 
VHSKHGDNGS NVGLKGWYGH DKSSRFLMDN KFVPTPGAQG FQCSNPSAVD LTCLAGSLSV 

       370        380        390        400        410        420 
FQKTSVADLR SRSLLLTAYA EHLLTQIASR NIKDGNFPFQ IISPLDPRFR GAQLSVLLQE 

       430        440        450        460        470        480 
DVMEEVFAGL EENGVICDKR KPGIIRVAPV PMYNTFEDVY KFMHILEGAL QPKAEQKTQA 


HGEAVEARL

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References

[1]"Dothideomycete-plant interactions illuminated by genome sequencing and EST analysis of the wheat pathogen Stagonospora nodorum."
Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L., Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E., Torriani S.F.F., McDonald B.A., Oliver R.P.
Plant Cell 19:3347-3368(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SN15 / ATCC MYA-4574 / FGSC 10173.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CH445328 Genomic DNA. Translation: EAT89545.1.
RefSeqXP_001793409.1. XM_001793357.1.

3D structure databases

ProteinModelPortalQ0UZK0.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSNOT_02814; SNOT_02814; SNOG_02814.
GeneID5970266.
KEGGpno:SNOG_02814.

Phylogenomic databases

KOK01556.
OMAMVSFYRP.
OrthoDBEOG4TB7KQ.

Enzyme and pathway databases

UniPathwayUPA00253; UER00329.
UPA00334; UER00455.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPMF_01970. Kynureninase.
InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR14084. PTHR14084. 1 hit.
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFPIRSF038800. KYNU. 1 hit.
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR01814. kynureninase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKYNU2_PHANO
AccessionPrimary (citable) accession number: Q0UZK0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: September 5, 2006
Last modified: March 6, 2013
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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